1tpl

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(New page: 200px<br /><applet load="1tpl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tpl, resolution 2.3&Aring;" /> '''THE THREE-DIMENSIONAL...)
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[[Image:1tpl.gif|left|200px]]<br /><applet load="1tpl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tpl, resolution 2.3&Aring;" />
 
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'''THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE'''<br />
 
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==Overview==
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==THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE==
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Tyrosine phenol-lyase (EC 4.1.99.2) from Citrobacter freundii has been, cloned and the primary sequence deduced from the DNA sequence. From the, BrCN digest of the NaBH4-reduced holoenzyme, five peptides were purified, and sequenced. The amino acid sequences of the peptides agreed with the, corresponding parts of the tyrosine phenol-lyase sequence obtained from, the gene structure. K257 is the pyridoxal 5'-phosphate binding residue., Assisted by the sequence data, the crystal structure of apotyrosine, phenol-lyase, a pyridoxal 5'-phosphate-dependent enzyme, has been refined, to an R-factor of 16.2% at 2.3-A resolution using synchrotron radiation, diffraction data. The tetrameric molecule has 222 symmetry, with one of, the axes coincident with the crystallographic 2-fold symmetry axis of the, crystal which belongs to the space group P2(1)2(1)2 with a = 76.0 A, b =, 138.3 A, and c = 93.5 A. Each subunit comprises 14 alpha-helices and 16, beta-strands, which fold into a small and a large domain. The, coenzyme-binding lysine residue is located at the interface between the, large and small domains of one subunit and the large domain of a, crystallographically related subunit. The fold of the large, pyridoxal, 5'-phosphate binding domain and the location of the active site are, similar to that found in aminotransferases. Most of the residues which, participate in binding of pyridoxal 5'-phosphate in aminotransferases are, conserved in the structure of tyrosine phenol-lyase. Two dimers of, tyrosine phenol-lyase, each of which has a domain architecture similar to, that found in aspartate aminotransferases, are bound together through a, hydrophobic cluster in the center of the molecule and intertwined, N-terminal arms.
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<StructureSection load='1tpl' size='340' side='right'caption='[[1tpl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tpl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_intermedius Citrobacter intermedius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TPL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tpl OCA], [https://pdbe.org/1tpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tpl RCSB], [https://www.ebi.ac.uk/pdbsum/1tpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tpl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPL_CITFR TPL_CITFR]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tp/1tpl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tpl ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TPL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tyrosine_phenol-lyase Tyrosine phenol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.2 4.1.99.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TPL OCA].
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*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Three-dimensional structure of tyrosine phenol-lyase., Antson AA, Demidkina TV, Gollnick P, Dauter Z, von Tersch RL, Long J, Berezhnoy SN, Phillips RS, Harutyunyan EH, Wilson KS, Biochemistry. 1993 Apr 27;32(16):4195-206. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7916622 7916622]
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[[Category: Citrobacter intermedius]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Tyrosine phenol-lyase]]
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[[Category: Antson A]]
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[[Category: Antson, A.]]
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[[Category: Dauter Z]]
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[[Category: Dauter, Z.]]
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[[Category: Demidkina T]]
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[[Category: Demidkina, T.]]
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[[Category: Harutyunyan E]]
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[[Category: Harutyunyan, E.]]
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[[Category: Wilson K]]
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[[Category: Wilson, K.]]
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[[Category: SO4]]
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[[Category: lyase(carbon-carbon)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:29:21 2007''
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Current revision

THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE

PDB ID 1tpl

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